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Protein

Pyruvate carboxylase 2

Gene

PYC2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.

Catalytic activityi

ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei137ATPBy similarity1
Binding sitei221ATPBy similarity1
Binding sitei256ATPBy similarity1
Active sitei313By similarity1
Metal bindingi567Divalent metal cationBy similarity1
Binding sitei639SubstrateBy similarity1
Metal bindingi735Divalent metal cation; via carbamate groupBy similarity1
Metal bindingi765Divalent metal cationBy similarity1
Metal bindingi767Divalent metal cationBy similarity1
Binding sitei899SubstrateBy similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • biotin binding Source: InterPro
  • biotin carboxylase activity Source: InterPro
  • DNA binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • pyruvate carboxylase activity Source: SGD

GO - Biological processi

  • gluconeogenesis Source: SGD
  • pyruvate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

ATP-binding, Biotin, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YBR218C-MONOMER.
BRENDAi6.4.1.1. 984.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate carboxylase 2 (EC:6.4.1.1)
Alternative name(s):
Pyruvic carboxylase 2
Short name:
PCB 2
Gene namesi
Name:PYC2
Ordered Locus Names:YBR218C
ORF Names:YBR1507
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR218C.
SGDiS000000422. PYC2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001468252 – 1180Pyruvate carboxylase 2Add BLAST1179

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei735N6-carboxylysineBy similarity1
Modified residuei1136N6-biotinyllysinePROSITE-ProRule annotationBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32327.
PRIDEiP32327.

PTM databases

iPTMnetiP32327.

Expressioni

Inductioni

By glucose.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi32915. 89 interactors.
DIPiDIP-6426N.
IntActiP32327. 2 interactors.
MINTiMINT-2781496.

Structurei

3D structure databases

ProteinModelPortaliP32327.
SMRiP32327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 471Biotin carboxylationAdd BLAST453
Domaini141 – 338ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini558 – 825Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST268
Domaini1095 – 1170Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni566 – 570Substrate bindingBy similarity5

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated
Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated
Contains 1 pyruvate carboxyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00860000133991.
HOGENOMiHOG000282801.
InParanoidiP32327.
KOiK01958.
OMAiVEHAMPG.
OrthoDBiEOG092C0BFY.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFiPIRSF001594. Pyruv_carbox. 1 hit.
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01235. pyruv_carbox. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32327-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSKKLAGL RDNFSLLGEK NKILVANRGE IPIRIFRSAH ELSMRTIAIY
60 70 80 90 100
SHEDRLSMHR LKADEAYVIG EEGQYTPVGA YLAMDEIIEI AKKHKVDFIH
110 120 130 140 150
PGYGFLSENS EFADKVVKAG ITWIGPPAEV IDSVGDKVSA RHLAARANVP
160 170 180 190 200
TVPGTPGPIE TVQEALDFVN EYGYPVIIKA AFGGGGRGMR VVREGDDVAD
210 220 230 240 250
AFQRATSEAR TAFGNGTCFV ERFLDKPKHI EVQLLADNHG NVVHLFERDC
260 270 280 290 300
SVQRRHQKVV EVAPAKTLPR EVRDAILTDA VKLAKVCGYR NAGTAEFLVD
310 320 330 340 350
NQNRHYFIEI NPRIQVEHTI TEEITGIDIV SAQIQIAAGA TLTQLGLLQD
360 370 380 390 400
KITTRGFSIQ CRITTEDPSK NFQPDTGRLE VYRSAGGNGV RLDGGNAYAG
410 420 430 440 450
ATISPHYDSM LVKCSCSGST YEIVRRKMIR ALIEFRIRGV KTNIPFLLTL
460 470 480 490 500
LTNPVFIEGT YWTTFIDDTP QLFQMVSSQN RAQKLLHYLA DLAVNGSSIK
510 520 530 540 550
GQIGLPKLKS NPSVPHLHDA QGNVINVTKS APPSGWRQVL LEKGPSEFAK
560 570 580 590 600
QVRQFNGTLL MDTTWRDAHQ SLLATRVRTH DLATIAPTTA HALAGAFALE
610 620 630 640 650
CWGGATFDVA MRFLHEDPWE RLRKLRSLVP NIPFQMLLRG ANGVAYSSLP
660 670 680 690 700
DNAIDHFVKQ AKDNGVDIFR VFDALNDLEQ LKVGVNAVKK AGGVVEATVC
710 720 730 740 750
YSGDMLQPGK KYNLDYYLEV VEKIVQMGTH ILGIKDMAGT MKPAAAKLLI
760 770 780 790 800
GSLRTRYPDL PIHVHSHDSA GTAVASMTAC ALAGADVVDV AINSMSGLTS
810 820 830 840 850
QPSINALLAS LEGNIDTGIN VEHVRELDAY WAEMRLLYSC FEADLKGPDP
860 870 880 890 900
EVYQHEIPGG QLTNLLFQAQ QLGLGEQWAE TKRAYREANY LLGDIVKVTP
910 920 930 940 950
TSKVVGDLAQ FMVSNKLTSD DIRRLANSLD FPDSVMDFFE GLIGQPYGGF
960 970 980 990 1000
PEPLRSDVLR NKRRKLTCRP GLELEPFDLE KIREDLQNRF GDIDECDVAS
1010 1020 1030 1040 1050
YNMYPRVYED FQKIRETYGD LSVLPTKNFL APAEPDEEIE VTIEQGKTLI
1060 1070 1080 1090 1100
IKLQAVGDLN KKTGQREVYF ELNGELRKIR VADKSQNIQS VAKPKADVHD
1110 1120 1130 1140 1150
THQIGAPMAG VIIEVKVHKG SLVKKGESIA VLSAMKMEMV VSSPADGQVK
1160 1170 1180
DVFIKDGESV DASDLLVVLE EETLPPSQKK
Length:1,180
Mass (Da):130,167
Last modified:October 1, 1994 - v2
Checksum:iAD60DA3A60F5E001
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti15S → C in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti132D → E in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti238N → K in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti268L → F in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti546S → C in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti642N → T in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti771 – 773GTA → STR in CAA42544 (PubMed:1921979).Curated3
Sequence conflicti831W → R in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti839S → P in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti1001Y → N in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti1155K → R in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti1178Q → P in CAA42544 (PubMed:1921979).Curated1
Sequence conflicti1180K → KVIFTR in CAA42544 (PubMed:1921979).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59890 Genomic DNA. Translation: CAA42544.1.
U35647 Genomic DNA. Translation: AAC49147.1.
Z36087 Genomic DNA. Translation: CAA85182.1.
BK006936 Genomic DNA. Translation: DAA07334.1.
PIRiS46094.
RefSeqiNP_009777.1. NM_001178566.1.

Genome annotation databases

EnsemblFungiiYBR218C; YBR218C; YBR218C.
GeneIDi852519.
KEGGisce:YBR218C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59890 Genomic DNA. Translation: CAA42544.1.
U35647 Genomic DNA. Translation: AAC49147.1.
Z36087 Genomic DNA. Translation: CAA85182.1.
BK006936 Genomic DNA. Translation: DAA07334.1.
PIRiS46094.
RefSeqiNP_009777.1. NM_001178566.1.

3D structure databases

ProteinModelPortaliP32327.
SMRiP32327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32915. 89 interactors.
DIPiDIP-6426N.
IntActiP32327. 2 interactors.
MINTiMINT-2781496.

PTM databases

iPTMnetiP32327.

Proteomic databases

MaxQBiP32327.
PRIDEiP32327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR218C; YBR218C; YBR218C.
GeneIDi852519.
KEGGisce:YBR218C.

Organism-specific databases

EuPathDBiFungiDB:YBR218C.
SGDiS000000422. PYC2.

Phylogenomic databases

GeneTreeiENSGT00860000133991.
HOGENOMiHOG000282801.
InParanoidiP32327.
KOiK01958.
OMAiVEHAMPG.
OrthoDBiEOG092C0BFY.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciYEAST:YBR218C-MONOMER.
BRENDAi6.4.1.1. 984.

Miscellaneous databases

PROiP32327.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFiPIRSF001594. Pyruv_carbox. 1 hit.
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01235. pyruv_carbox. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYC2_YEAST
AccessioniPrimary (citable) accession number: P32327
Secondary accession number(s): D6VQL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1994
Last modified: November 30, 2016
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 17000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.